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Related Experiment Video

Updated: Oct 15, 2025

Biomimetic Materials to Characterize Bacteria-host Interactions

Biomimetic Materials to Characterize Bacteria-host Interactions

Published on: November 16, 2015

Full-Length Galectin-3 Is Required for High Affinity Microbial Interactions and Antimicrobial Activity.

Shang-Chuen Wu¹, Alex D Ho¹, Nourine A Kamili²

¹Joint Program in Transfusion Medicine, Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States.

Frontiers in Microbiology

|October 25, 2021

Summary

Galectin-3 (Gal-3) binds to self-like microbial antigens, offering innate immunity. While Gal-3

Keywords:

antimicrobial blood group galectin microbe molecular mimicry

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Last Updated: Oct 15, 2025

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Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads

Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads

Published on: December 9, 2020

Area of Science:

Immunology
Microbiology
Glycobiology

Background:

Adaptive immunity recognizes diverse antigens, but self-tolerance prevents autoimmunity.
Molecular mimicry, where microbes display self-like antigens, evades immune detection.
Galectins, particularly galectin-4 and galectin-8, are implicated in innate immunity against molecular mimicry.

Purpose of the Study:

To investigate the binding specificity and antimicrobial activity of human galectin-3 (Gal-3).
To explore the role of Gal-3 in recognizing microbial glycans that mimic self-antigens.

Main Methods:

Utilized glycan microarrays to assess Gal-3 and its C-terminal domain (Gal-3C) binding to mammalian and microbial glycans.
Tested Gal-3 and Gal-3C interactions with intact microbial strains expressing specific antigens.
Evaluated the antimicrobial activity of Gal-3 and Gal-3C against targeted bacteria.

Main Results:

Gal-3 demonstrated high binding to mammalian blood group A, B, and αGal antigens.
Both Gal-3 and Gal-3C specifically engaged distinct microbial glycans, with Gal-3 showing stronger binding.
Gal-3 and Gal-3C binding predicted interactions with intact microbes, including specific strains of *Providentia alcalifaciens* and *Klebsiella pneumoniae* expressing mammalian-like antigens.
Only Gal-3 exhibited antimicrobial activity against these bacteria, not Gal-3C.

Conclusions:

Galectin-3 specifically recognizes both mammalian and microbial glycans that mimic self-antigens.
The C-terminal domain of Gal-3 (Gal-3C) mediates glycan binding but lacks antimicrobial function.
Gal-3 possesses antimicrobial activity against bacteria employing molecular mimicry, highlighting its role in innate immunity.